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8 documents found
1: Title: A novel mutation in nuclear prelamin a recognition factor-like causes diffuse pulmonary arteriovenous malformations.
Authors: Liu, Hong-Zhou, et.al. .
Journal: Oncotarget, Vol. 8 (2): 2708-2718, 2017 .
Snippet: Furthermore, NARFL-knockdown cell lines demonstrated decreased activity of cytosolic aconitase, while NARFL-knockout zebrafish presented ectopic subintestinal vessels sprouts and upregulated VEGF.
Affiliation: Center for Gene Diagnosis, Zhongnan Hospital of Wuhan University, Wuhan, Hubei, 430071, China. Department of Pneumology, Zhongnan Hospital of Wuhan University, Wuhan, Hubei, 430071, China. Key Laboratory of Aquatic Biodiversity and Conservation of Chinese Academy of Sciences, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, Hubei, China. .
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2: Title: The iron-sulfur cluster assembly network component NARFL is a key element in the cellular defense against oxidative stress.
Authors: Corbin, Monique V, et.al. .
Journal: Free radical biology & medicine (Free Radic Biol Med), Vol. 89, 2015 .
Snippet: In line with this result we found the cytosolic c-aconitase activity as well as the nuclear protein RTEL1, both Fe-S dependent proteins, to be protected by NARFL overexpression under hyperoxia.
Affiliation: Department of Clinical Genetics, Section Oncogenetics, VU University Medical Center, 1081BT Amsterdam, The Netherlands. Electronic address: m.corbin@vumc.nl. Department of Clinical Genetics, Section Oncogenetics, VU University Medical Center, 1081BT Amsterdam, The Netherlands. Electronic address: rockx@vumc.nl. Department of Clinical Genetics, Section Oncogenetics, VU University Medical Center, 1081BT Amsterdam, The Netherlands. Electronic address: ab.oostra@vumc.nl. Department of Clinical Genetics, Section Oncogenetics, VU University Medical Center, 1081BT Amsterdam, The Netherlands. Electronic address: h.joenje@vumc.nl. Department of Clinical Genetics, Section Oncogenetics, VU University Medical Center, 1081BT Amsterdam, The Netherlands. Electronic address: jc.dorsman@vumc.nl. .
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3: Title: IOP1 protein is an external component of the human cytosolic iron-sulfur cluster assembly (CIA) machinery and functions in the MMS19 protein-dependent CIA pathway.
Authors: Seki, Mineaki, et.al. .
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 288 (23): 16680-9, 2013 .
Snippet: Recent studies have revealed that MMS19 and cytosolic iron-sulfur cluster assembly (CIA) factors form a complex and have central roles in CIA pathway.
Affiliation: Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan. mseki@fbs.osaka-u.ac.jp .
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4: Title: MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.
Authors: Gari, Kerstin, et.al. .
Journal: Science (New York, N.Y.) (Science), Vol. 337 (6091): 243-5, 2012 .
Snippet: in the absence of MMS19, a failure to transfer Fe-S clusters to target proteins is associated with Fe-S protein instability and preimplantation death of mice in which Mms19 has been knocked out; propose that MMS19 functions as a platform to facilitate Fe-S cluster transfer to proteins critical for DNA replication and repair
Affiliation: DNA Damage Response Laboratory, London Research Institute, Cancer Research UK, Clare Hall, South Mimms EN6 3LD, UK. .
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5: Title: Mouse knock-out of IOP1 protein reveals its essential role in mammalian cytosolic iron-sulfur protein biogenesis.
Authors: Song, Daisheng, et.al. .
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 286 (18): 15797-805, 2011 .
Snippet: Iron-only hydrogenase-like protein 1 (IOP1; also known as nuclear prelamin A recognition factor like protein, or NARFL) is a human protein that is homologous to Nar1, a protein in Saccharomyces cerevisiae that, in turn, is an essential component of the cytosolic iron-sulfur protein assembly pathway in yeast.
Affiliation: Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA. .
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6: Title: Human ISCA1 interacts with IOP1/NARFL and functions in both cytosolic and mitochondrial iron-sulfur protein biogenesis.
Authors: Song, Daisheng, et.al. .
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 284 (51): 35297-307, 2009 .
Snippet: We find that IscA1 interacts with IOP1 (iron-only hydrogenase-like protein 1)/NARFL (nuclear prelamin A recognition factor-like), a cytosolic protein that plays a role in the cytosolic iron-sulfur protein assembly pathway.
Affiliation: Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA. .
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7: Title: A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis.
Authors: Song, Daisheng, et.al. .
Journal: The Journal of biological chemistry (J Biol Chem), Vol. 283 (14): 9231-8, 2008 .
Snippet: We found that knockdown of IOP1 in both HeLa and Hep3B cells decreases the activity of cytosolic aconitase, an Fe-S protein, but not that of mitochondrial aconitase.
Affiliation: Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, 422 Curie Boulevard, Philadelphia, PA 19104, USA. .
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8: Title: IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1alpha activity.
Authors: Huang, Jianhe, et.al. .
Journal: The Biochemical journal (Biochem J), Vol. 401 (1): 341-52, 2007 .
Snippet: Knockdown of IOP1 using siRNA (small interfering RNA) in mammalian cells increases protein levels of HIF-1alpha under both normoxic and hypoxic conditions, and augments hypoxia-induced HRE (hypoxia response element) reporter gene and endogenous HIF-1alpha target gene expressions.
Affiliation: Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. .
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